ID W5Q8S5_SHEEP Unreviewed; 942 AA.
AC W5Q8S5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=ERAP1 {ECO:0000313|Ensembl:ENSOARP00000019117.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000019117.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000019117.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000019117.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000019117.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AMGL01094758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01094759; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004009139.1; XM_004009090.3.
DR AlphaFoldDB; W5Q8S5; -.
DR SMR; W5Q8S5; -.
DR STRING; 9940.ENSOARP00000019117; -.
DR MEROPS; M01.018; -.
DR PaxDb; 9940-ENSOARP00000019117; -.
DR Ensembl; ENSOART00000019385.1; ENSOARP00000019117.1; ENSOARG00000017807.1.
DR GeneID; 101110506; -.
DR KEGG; oas:101110506; -.
DR CTD; 51752; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_1_1; -.
DR OMA; MENWGVV; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000002356; Chromosome 5.
DR Bgee; ENSOARG00000017807; Expressed in jejunum and 51 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF156; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..942
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004870376"
FT DOMAIN 61..247
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 282..486
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 598..917
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 439
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 942 AA; 107052 MW; 42BAE9ACE5F80E25 CRC64;
MIPPSVKWPL ATRPLLLSTL LILLTVATPS SCQSREPTFP KASNGAPFPW NKMRLPEHII
PAHYDLMIHA NLTTLTFGGT TQIEITASEP TSTIILHSHH LQVSKATLRK GGGERQAEEP
LRVLENPPQE QIALLASKPL VVGLPYTIVI DYTGNLSESF HGFYKSTYRT KEGEVRVLAS
TQFEPTAARM AFPCFDEPAF KASFLIKIRR EPRHLAISNM PLVKSVIVAE GLIEDHFDVT
VKMSTYLVAF IVSDFKSVSK MTKSGVKVSV YAVPDKINQA DYALDAAVTL LEFYEDYFNI
PYPLPKQDLA AIPDFQSGAM ENWGLTTYRE SSLLFDAEKS SASSKLGITM TVSHELAHQW
FGNLVTMEWW NDLWLNEGFA KFMEFVSVSV THPELKVEEY FFGKCFNAME VDALNSSHPV
STPVENPAQI QEMFDEVSYE KGACILNMLR DYLGADAFKS GIVKYLQKYS YKNTKNEDLW
NSMASICPTD DTQHMDGFCS RGEHSSSTVH WRREGLDVKT MMNTWTLQKG FPLITITVRG
RNAHVKQEYY VKGVADAPET GLLWHIPLTF ITSKSDAVQR FLLKTRTDVL ILPEEVEWIK
FNVGMNGYYI VHYEDDGWDS LTGLLKGTHT AISSNDRASL INNAFQLVSI GKLSIEKALD
LTLYLKHETE IMPVFQGLNE LIPMYKLMEK REMNEVETQF KAFLIRLLRG LIDKQTWTDE
GSVSERMLRS QLLLLACVRK YQPCVQKAEG YFRQWQEAGG NLSLPNDVTL AVFAVGAQTL
EGWDFLYSKY QSSLSSTEKN QIEFALCISQ NKEKLQWLLD QSFKGDVIKT QEFPGILRAI
GRNPVGYLLA WQFLRENWNK LVQKFELGSS SIAYMVTGTT NQFSTRARLE EVKEFFSSLK
ENGSQLRCVQ QTIETIEENI RWMDKNFDKI KAWLQNEQLN LL
//
